期刊
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
卷 72, 期 -, 页码 22-33出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2059798315021142
关键词
VgrG1; T6SS; secretion; virulence; effectors; toxins; infection; P. aeruginosa; structure; X-ray crystallography
资金
- Spanish Ministry of Science and Innovation [BFU2011-24615, BFU2014-55448-P, CSD2009-00088]
- Regional Government of Madrid [S2010/BMD-2353]
- European Community's Seventh Framework Programme under BioStructX-5959 [283570]
The type VI secretion system (T6SS) is a mechanism that is commonly used by pathogenic bacteria to infect host cells and for survival in competitive environments. This system assembles on a core baseplate and elongates like a phage puncturing device; it is thought to penetrate the target membrane and deliver effectors into the host or competing bacteria. Valine-glycine repeat protein G1 (VgrG1) forms the spike at the tip of the elongating tube formed by haemolysin co-regulated protein 1 (Hcp1); it is structurally similar to the T4 phage (gp27)(3 3)-(gp5)(3 3) puncturing complex. Here, the crystal structure of full-length VgrG1 fromPseudomonas aeruginosa Pseudomonas aeruginosa is reported at a resolution of 2.0 angstrom, which through a trimeric arrangement generates a needle-like shape composed of two main parts, the head and the spike, connectedvia via a small neck region. The structure reveals several remarkable structural features pointing to the possible roles of the two main segments of VgrG1: the head as a scaffold cargo domain and the -roll spike with implications in the cell-membrane puncturing process and as a carrier of cognate toxins.
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